메뉴 건너뛰기




Volumn 20, Issue 5, 2012, Pages 814-825

The molecular architecture of the eukaryotic chaperonin TRiC/CCT

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONIN CONTAINING TCP1;

EID: 84861102204     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2012.03.007     Document Type: Article
Times cited : (241)

References (45)
  • 1
    • 0035783161 scopus 로고    scopus 로고
    • Gene duplication and the evolution of group II chaperonins: Implications for structure and function
    • J.M. Archibald, C. Blouin, and W.F. Doolittle Gene duplication and the evolution of group II chaperonins: implications for structure and function J. Struct. Biol. 135 2001 157 169
    • (2001) J. Struct. Biol. , vol.135 , pp. 157-169
    • Archibald, J.M.1    Blouin, C.2    Doolittle, W.F.3
  • 2
    • 77954257799 scopus 로고    scopus 로고
    • ConSurf 2010: Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • Web Server Issue
    • H. Ashkenazy, E. Erez, E. Martz, T. Pupko, and N. Ben-Tal ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids Nucleic Acids Res. 38 Web Server issue 2010 W529 W533
    • (2010) Nucleic Acids Res. , vol.38
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5
  • 8
    • 79961026866 scopus 로고    scopus 로고
    • The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins
    • C. Dekker, S.M. Roe, E.A. McCormack, F. Beuron, L.H. Pearl, and K.R. Willison The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins EMBO J. 30 2011 3078 3090
    • (2011) EMBO J. , vol.30 , pp. 3078-3090
    • Dekker, C.1    Roe, S.M.2    McCormack, E.A.3    Beuron, F.4    Pearl, L.H.5    Willison, K.R.6
  • 9
    • 0032478545 scopus 로고    scopus 로고
    • Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT
    • DOI 10.1016/S0092-8674(00)81152-6
    • L. Ditzel, J. Löwe, D. Stock, K.O. Stetter, H. Huber, R. Huber, and S. Steinbacher Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT Cell 93 1998 125 138 (Pubitemid 28173558)
    • (1998) Cell , vol.93 , Issue.1 , pp. 125-138
    • Ditzel, L.1    Lowe, J.2    Stock, D.3    Stetter, K.-O.4    Huber, H.5    Huber, R.6    Steinbacher, S.7
  • 10
    • 78651499753 scopus 로고    scopus 로고
    • Dual action of ATP hydrolysis couples lid closure to substrate release into the group II chaperonin chamber
    • N.R. Douglas, S. Reissmann, J. Zhang, B. Chen, J. Jakana, R. Kumar, W. Chiu, and J. Frydman Dual action of ATP hydrolysis couples lid closure to substrate release into the group II chaperonin chamber Cell 144 2011 240 252
    • (2011) Cell , vol.144 , pp. 240-252
    • Douglas, N.R.1    Reissmann, S.2    Zhang, J.3    Chen, B.4    Jakana, J.5    Kumar, R.6    Chiu, W.7    Frydman, J.8
  • 12
    • 0345708112 scopus 로고    scopus 로고
    • Tumorigenic mutations in VHL disrupt folding in vivo by interfering with chaperonin binding
    • DOI 10.1016/S1097-2765(03)00423-4
    • D.E. Feldman, C. Spiess, D.E. Howard, and J. Frydman Tumorigenic mutations in VHL disrupt folding in vivo by interfering with chaperonin binding Mol. Cell 12 2003 1213 1224 (Pubitemid 37487929)
    • (2003) Molecular Cell , vol.12 , Issue.5 , pp. 1213-1224
    • Feldman, D.E.1    Spiess, C.2    Howard, D.E.3    Frydman, J.4
  • 13
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • F.U. Hartl, A. Bracher, and M. Hayer-Hartl Molecular chaperones in protein folding and proteostasis Nature 475 2011 324 332
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 15
    • 79961213851 scopus 로고    scopus 로고
    • Structural analysis of a prokaryotic ribosome using a novel amidinating cross-linker and mass spectrometry
    • M.A. Lauber, and J.P. Reilly Structural analysis of a prokaryotic ribosome using a novel amidinating cross-linker and mass spectrometry J. Proteome Res. 10 2011 3604 3616
    • (2011) J. Proteome Res. , vol.10 , pp. 3604-3616
    • Lauber, M.A.1    Reilly, J.P.2
  • 17
    • 84857966803 scopus 로고    scopus 로고
    • Expanding the chemical cross-linking toolbox by the use of multiple proteases and enrichment by size exclusion chromatography
    • M111.014126
    • A. Leitner, R. Reischl, T. Walzthoeni, F. Herzog, S. Bohn, F. Förster, and R. Aebersold Expanding the chemical cross-linking toolbox by the use of multiple proteases and enrichment by size exclusion chromatography Mol. Cell. Proteomics 11 2012 M111.014126
    • (2012) Mol. Cell. Proteomics , vol.11
    • Leitner, A.1    Reischl, R.2    Walzthoeni, T.3    Herzog, F.4    Bohn, S.5    Förster, F.6    Aebersold, R.7
  • 18
    • 0030842428 scopus 로고    scopus 로고
    • Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT micro-complexes
    • DOI 10.1093/emboj/16.14.4311
    • A.K. Liou, and K.R. Willison Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT micro-complexes EMBO J. 16 1997 4311 4316 (Pubitemid 27298184)
    • (1997) EMBO Journal , vol.16 , Issue.14 , pp. 4311-4316
    • Liou, A.K.F.1    Willison, K.R.2
  • 25
    • 0038737003 scopus 로고    scopus 로고
    • Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis
    • DOI 10.1016/S0092-8674(03)00307-6
    • A.S. Meyer, J.R. Gillespie, D. Walther, I.S. Millet, S. Doniach, and J. Frydman Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis Cell 113 2003 369 381 (Pubitemid 36556118)
    • (2003) Cell , vol.113 , Issue.3 , pp. 369-381
    • Meyer, A.S.1    Gillespie, J.R.2    Walther, D.3    Millet, I.S.4    Doniach, S.5    Frydman, J.6
  • 26
    • 0035326345 scopus 로고    scopus 로고
    • Isotope-tagged cross-linking reagents. A new tool in mass spectrometric protein interaction analysis
    • DOI 10.1021/ac001379a
    • D.R. Müller, P. Schindler, H. Towbin, U. Wirth, H. Voshol, S. Hoving, and M.O. Steinmetz Isotope-tagged cross-linking reagents. A new tool in mass spectrometric protein interaction analysis Anal. Chem. 73 2001 1927 1934 (Pubitemid 32862396)
    • (2001) Analytical Chemistry , vol.73 , Issue.9 , pp. 1927-1934
    • Muller, D.R.1    Schindler, P.2    Towbin, H.3    Wirth, U.4    Voshol, H.5    Hoving, S.6    Steinmetz, M.O.7
  • 30
    • 78149438179 scopus 로고    scopus 로고
    • Crosslinking combined with mass spectrometry for structural proteomics
    • E.V. Petrotchenko, and C.H. Borchers Crosslinking combined with mass spectrometry for structural proteomics Mass Spectrom. Rev. 29 2010 862 876
    • (2010) Mass Spectrom. Rev. , vol.29 , pp. 862-876
    • Petrotchenko, E.V.1    Borchers, C.H.2
  • 31
    • 0002218484 scopus 로고    scopus 로고
    • Rate4Site: An algorithmic tool for the identification of functional regions in proteins by surface mapping of evolutionary determinants within their homologues
    • T. Pupko, R.E. Bell, I. Mayrose, F. Glaser, and N. Ben-Tal Rate4Site: an algorithmic tool for the identification of functional regions in proteins by surface mapping of evolutionary determinants within their homologues Bioinformatics 18 Suppl 1 2002 S71 S77
    • (2002) Bioinformatics , vol.18 , Issue.SUPPL. 1
    • Pupko, T.1    Bell, R.E.2    Mayrose, I.3    Glaser, F.4    Ben-Tal, N.5
  • 32
    • 79851513173 scopus 로고    scopus 로고
    • The beginning of a beautiful friendship: Cross-linking/mass spectrometry and modelling of proteins and multi-protein complexes
    • J. Rappsilber The beginning of a beautiful friendship: cross-linking/mass spectrometry and modelling of proteins and multi-protein complexes J. Struct. Biol. 173 2011 530 540
    • (2011) J. Struct. Biol. , vol.173 , pp. 530-540
    • Rappsilber, J.1
  • 33
    • 34247635168 scopus 로고    scopus 로고
    • Essential function of the built-in lid in the allosteric regulation of eukaryotic and archaeal chaperonins
    • DOI 10.1038/nsmb1236, PII NSMB1236
    • S. Reissmann, C. Parnot, C.R. Booth, W. Chiu, and J. Frydman Essential function of the built-in lid in the allosteric regulation of eukaryotic and archaeal chaperonins Nat. Struct. Mol. Biol. 14 2007 432 440 (Pubitemid 46685886)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.5 , pp. 432-440
    • Reissmann, S.1    Parnot, C.2    Booth, C.R.3    Chiu, W.4    Frydman, J.5
  • 35
    • 17844378217 scopus 로고    scopus 로고
    • Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis
    • DOI 10.1038/nsmb901
    • D. Rivenzon-Segal, S.G. Wolf, L. Shimon, K.R. Willison, and A. Horovitz Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis Nat. Struct. Mol. Biol. 12 2005 233 237 (Pubitemid 43079364)
    • (2005) Nature Structural and Molecular Biology , vol.12 , Issue.3 , pp. 233-237
    • Rivenzon-Segal, D.1    Wolf, S.G.2    Shimon, L.3    Willison, K.R.4    Horovitz, A.5
  • 37
    • 34548749239 scopus 로고    scopus 로고
    • Annexin A2/P11 interaction: New insights into annexin A2 tetramer structure by chemical crosslinking, high-resolution mass spectrometry, and computational modeling
    • DOI 10.1002/prot.21445
    • D.M. Schulz, S. Kalkhof, A. Schmidt, C. Ihling, C. Stingl, K. Mechtler, O. Zschörnig, and A. Sinz Annexin A2/P11 interaction: new insights into annexin A2 tetramer structure by chemical crosslinking, high-resolution mass spectrometry, and computational modeling Proteins 69 2007 254 269 (Pubitemid 47429289)
    • (2007) Proteins: Structure, Function and Genetics , vol.69 , Issue.2 , pp. 254-269
    • Schulz, D.M.1    Kalkhof, S.2    Schmidt, A.3    Ihling, C.4    Stingl, C.5    Mechtler, K.6    Zschornig, O.7    Sinz, A.8
  • 38
    • 0347757092 scopus 로고    scopus 로고
    • Crystal Structures of the Group II Chaperonin from Thermococcus strain KS-1: Steric Hindrance by the Substituted Amino Acid, and Inter-subunit Rearrangement between Two Crystal Forms
    • DOI 10.1016/j.jmb.2003.11.028
    • Y. Shomura, T. Yoshida, R. Iizuka, T. Maruyama, M. Yohda, and K. Miki Crystal structures of the group II chaperonin from Thermococcus strain KS-1: steric hindrance by the substituted amino acid, and inter-subunit rearrangement between two crystal forms J. Mol. Biol. 335 2004 1265 1278 (Pubitemid 38081291)
    • (2004) Journal of Molecular Biology , vol.335 , Issue.5 , pp. 1265-1278
    • Shomura, Y.1    Yoshida, T.2    Iizuka, R.3    Maruyama, T.4    Yohda, M.5    Miki, K.6
  • 39
    • 33745742438 scopus 로고    scopus 로고
    • Chemical cross-linking and mass spectrometry to map three-dimensional protein structures and protein-protein interactions
    • DOI 10.1002/mas.20082
    • A. Sinz Chemical cross-linking and mass spectrometry to map three-dimensional protein structures and protein-protein interactions Mass Spectrom. Rev. 25 2006 663 682 (Pubitemid 44014105)
    • (2006) Mass Spectrometry Reviews , vol.25 , Issue.4 , pp. 663-682
    • Sinz, A.1
  • 40
    • 7444231693 scopus 로고    scopus 로고
    • Mechanism of the eukaryotic chaperonin: Protein folding in the chamber of secrets
    • DOI 10.1016/j.tcb.2004.09.015, PII S0962892404002661
    • C. Spiess, A.S. Meyer, S. Reissmann, and J. Frydman Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets Trends Cell Biol. 14 2004 598 604 (Pubitemid 39440608)
    • (2004) Trends in Cell Biology , vol.14 , Issue.11 , pp. 598-604
    • Spiess, C.1    Meyer, A.S.2    Reissmann, S.3    Frydman, J.4
  • 41
    • 33749080319 scopus 로고    scopus 로고
    • Identification of the TRiC/CCT Substrate Binding Sites Uncovers the Function of Subunit Diversity in Eukaryotic Chaperonins
    • DOI 10.1016/j.molcel.2006.09.003, PII S1097276506006319
    • C. Spiess, E.J. Miller, A.J. McClellan, and J. Frydman Identification of the TRiC/CCT substrate binding sites uncovers the function of subunit diversity in eukaryotic chaperonins Mol. Cell 24 2006 25 37 (Pubitemid 44466686)
    • (2006) Molecular Cell , vol.24 , Issue.1 , pp. 25-37
    • Spiess, C.1    Miller, E.J.2    McClellan, A.J.3    Frydman, J.4
  • 42
    • 44349090822 scopus 로고    scopus 로고
    • Essential role of the chaperonin folding compartment in vivo
    • DOI 10.1038/emboj.2008.77, PII EMBOJ200877
    • Y.C. Tang, H.C. Chang, K. Chakraborty, F.U. Hartl, and M. Hayer-Hartl Essential role of the chaperonin folding compartment in vivo EMBO J. 27 2008 1458 1468 (Pubitemid 351733332)
    • (2008) EMBO Journal , vol.27 , Issue.10 , pp. 1458-1468
    • Tang, Y.-C.1    Chang, H.-C.2    Chakraborty, K.3    Hartl, F.U.4    Hayer-Hartl, M.5
  • 43
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • J.D. Thompson, D.G. Higgins, and T.J. Gibson CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res. 22 1994 4673 4680 (Pubitemid 24354800)
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 44
    • 57149098022 scopus 로고    scopus 로고
    • Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies
    • A.Y. Yam, Y. Xia, H.T. Lin, A. Burlingame, M. Gerstein, and J. Frydman Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies Nat. Struct. Mol. Biol. 15 2008 1255 1262
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1255-1262
    • Yam, A.Y.1    Xia, Y.2    Lin, H.T.3    Burlingame, A.4    Gerstein, M.5    Frydman, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.